Characterization of soluble artificial proteins with random sequences.
The structural and catalytic properties of two soluble random proteins, RP3-42 and RP3-45, of 141 amino acid residues were investigated. Although no marked secondary structure was detected by CD spectrum, sedimentation equilibrium and small-angle X-ray scattering studies showed that they form an oligomeric structure and are as compact as the molten globule. The random proteins have low but distinct esterase activity; the values of the second-order rate constant for the hydrolysis of p-nitrophenol were 0.78 and 1.39 M(-1) s(-1) for RP3-42 and RP3-45, respectively. The differences in the properties of the random and the native proteins are discussed from the evolutionary point of view.
Yamauchi
A
A
Department of Biotechnology, Faculty of Engineering, Osaka University, Suita, Japan.
Yomo
T
T
Tanaka
F
F
Prijambada
I D
ID
Ohhashi
S
S
Yamamoto
K
K
Shima
Y
Y
Ogasahara
K
K
Yutani
K
K
Kataoka
M
M
Urabe
I
I
D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D002384:Catalysis; D011232:Chemical Precipitation; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012995:Solubility
D009842:Oligopeptides; D011506:Proteins; D000645:Ammonium Sulfate